NUD17_ARATH
ID NUD17_ARATH Reviewed; 182 AA.
AC Q9ZU95; Q8L979;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Nudix hydrolase 17, mitochondrial;
DE Short=AtNUDT17;
DE EC=3.6.1.-;
DE Flags: Precursor;
GN Name=NUDT17; Synonyms=NUDX17; OrderedLocusNames=At2g01670;
GN ORFNames=T8O11.16;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NOMENCLATURE.
RX PubMed=15878881; DOI=10.1074/jbc.m503536200;
RA Ogawa T., Ueda Y., Yoshimura K., Shigeoka S.;
RT "Comprehensive analysis of cytosolic nudix hydrolases in Arabidopsis
RT thaliana.";
RL J. Biol. Chem. 280:25277-25283(2005).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=18815383; DOI=10.1104/pp.108.128413;
RA Ogawa T., Yoshimura K., Miyake H., Ishikawa K., Ito D., Tanabe N.,
RA Shigeoka S.;
RT "Molecular characterization of organelle-type Nudix hydrolases in
RT Arabidopsis.";
RL Plant Physiol. 148:1412-1424(2008).
CC -!- FUNCTION: Probably mediates the hydrolysis of some nucleoside
CC diphosphate derivatives. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and
CC inflorescences. {ECO:0000269|PubMed:18815383}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM66124.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC006069; AAD12704.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05483.1; -; Genomic_DNA.
DR EMBL; AF325062; AAK17130.1; -; mRNA.
DR EMBL; AF360131; AAK25841.1; -; mRNA.
DR EMBL; AF412103; AAL06556.1; -; mRNA.
DR EMBL; AY051030; AAK93707.1; -; mRNA.
DR EMBL; AY088595; AAM66124.1; ALT_INIT; mRNA.
DR PIR; F84427; F84427.
DR RefSeq; NP_565273.1; NM_126228.5.
DR AlphaFoldDB; Q9ZU95; -.
DR SMR; Q9ZU95; -.
DR STRING; 3702.AT2G01670.1; -.
DR PaxDb; Q9ZU95; -.
DR PRIDE; Q9ZU95; -.
DR ProteomicsDB; 226030; -.
DR EnsemblPlants; AT2G01670.1; AT2G01670.1; AT2G01670.
DR GeneID; 814696; -.
DR Gramene; AT2G01670.1; AT2G01670.1; AT2G01670.
DR KEGG; ath:AT2G01670; -.
DR Araport; AT2G01670; -.
DR TAIR; locus:2065440; AT2G01670.
DR eggNOG; KOG2839; Eukaryota.
DR HOGENOM; CLU_037162_5_2_1; -.
DR InParanoid; Q9ZU95; -.
DR OMA; YVMLIQS; -.
DR OrthoDB; 1324716at2759; -.
DR PhylomeDB; Q9ZU95; -.
DR BioCyc; ARA:AT2G01670-MON; -.
DR PRO; PR:Q9ZU95; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZU95; baseline and differential.
DR Genevisible; Q9ZU95; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Mitochondrion;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..182
FT /note="Nudix hydrolase 17, mitochondrial"
FT /id="PRO_0000019960"
FT DOMAIN 27..158
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 65..86
FT /note="Nudix box"
FT BINDING 80
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CONFLICT 1
FT /note="M -> I (in Ref. 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 182 AA; 21052 MW; 2C07EBAA5360B576 CRC64;
MGVEKMVCLA SRTGRQFQRY NKGRRQVVGC VPYRFKLSND GKISDEVEVL VISSQKGHAL
MFPKGGWELD ESVEEAASRE CLEEAGVLGN VEHQLGKWDF LSKSRGTYYE GLMFPMLVTE
QLELWPEQHV RQRIWMNVTE AREACRDWWM KEALDVLVER LSSPMNQPKE EKTMSISIET
MC
